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. 2017 Apr 20;7:992. doi: 10.1038/s41598-017-01019-5

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Design and in vitro characterization of IgG4Δhinge. (a) Sequence alignment of residues 205–234 (EU-numbering convention) of human IgG1, IgG4 and IgG4Δhinge. (b) Purified human IgG1, IgG4 and IgG4Δhinge variants of mAb 637 analyzed by non-reducing SDS-PAGE (image is cropped to show relevant bands, the complete gel is shown in supplementary Fig. 5). (c) In silico model of IgG4Δhinge based on crystal structures 1ADQ⁶¹ (CH2-CH3 domains), 1MCO⁶² (Δhinge region) and 1HZH⁶³ (Fab region). HCΔhinge depicted in green, LC depicted in pale green. (d) AChR surface down-modulation on TE671 cells by purified variants of mAb 637 as indicated. Pooled intravenous immunoglobulin (IVIg) is included as negative control (e) Inhibition of (auto-) antibody-mediated AChR surface down-modulation on TE671 cells by IgG4Δhinge-637. Different concentrations of the challenge autoantibody (IgG1-637) or a negative control (IVIG) were tested in combination with IgG4Δhinge-637; each curve corresponds to a single concentration of challenge antibody (0–10 nM) as shown in the key on the right.